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Creutzfeldt-Jakob disease (CJD) is a terminal brain disease with crippling symptoms that cause a slow weakening of the nervous system. The illness is contagious and has infected many people in American society. The Creutzfeldt-Jakob disease is caused by an abnormally occurring and extremely communicable enzyme in the brain known as a prion. Both animals and humans are affected by the disease. Cases of disease spread have been on the rise in recent years due to their high-risk aspect and despite the modes of communicable nature. Imperatively, previous and current research both attempt to outline the nature and structures of the prions that are believed to be the causal agents of the disease. Controversies, however, have been raised concerning the forms of transmission of the disease and the relationship between the disease in both humans and animals. The paper will outline the structure of the prions, the transmission of the disease and the difficulties encountered in the sterilization of equipment contaminated by the CJD prions.

Nature and Structure of Prions

The proteins with prions (PrP) are found entirely on the body of both healthy persons and animals. Conversely, PrP set up in transmittable material has a diverse structure and it is resilient to the proteases, which is an enzyme in the body that breaks down proteins. Prions are communicable proteins which have the shortage of nucleic acids (Enger et al., 21). The structural form of this PrPSc protein shows that it contains two entwined fibrils that are likely to comprise of series of the repeated beta-strands or some rungs which are called beta-solenoid. The structure gives some clues on how the pathogenic prion protein alters any normal PrPC into a PrPSc (Enger et al., 22). The lower and the upper rungs of the beta-solenoids are the likely the start points for the hydrogen-bonding with the later PrPC molecules found in the numerous proteins with the beta-solenoids, then they are choked up to avert the propagation of the beta-sheets (Tycko, 64). When added to some of the fibrils, the results would aid in the process of recruiting the extra proteins, and these chains lengthen.

The form of the usual PrPC protein, showed some time back, exposed that it is mainly alpha-helical with tiny beta-strand contents. The structure of the PrPSc protein is shown to be elusive since it forms combinations and the amyloid fibrils (Gendoo, 16). It has been established that the PrPSc protein contains extra beta-strand contents than the usual protein; however how this asset would result in the prion replication was not revealed clearly. Research has found more on the structure of the prion due to the frequent practice of technological usage.

However, the structural form of the PrPSc protein has been identified by the cryo-electron microscopy which has helped in the image reconstruction. This protein was cleansed from the transgenic mice encoded to create a form of the PrPSc protein which is not fixed to a cell membrane, which is under-glycosylated. The protein is shown to causes illness in the mice but is further consistent and forms the febrile plaques, permitting gentler sanitization methods.

Spongiform encephalopathy is neurodegenerative illnesses triggered by the miscoding of the cellular prion proteins. Spongiform encephalopathies found in humans are categorized into three kinds: communicable, ancestral or hereditary, and intermittent, illustrious by what method the disease is attained initially. Usually, the pathogenic protein encoded as PrPC protein having a different conformation, known as PrPsc. In the simple case, the PrPSc alters the normal PrPC protein to form many duplicates of the pathogenic system.

Many authors have noted that these molecular connections that control the prion templates, including the hydrogen-bonding, are charged and these hydrophobic interactions, the aromatic piling, and the steric restraints play critical roles in the DNA replication. The structural form of the PrPSc protein creates a mechanism for the prion replications through the combination of extra molecules into the budding beta-solenoid.

Transmission of Creutzfeldt - Jakob Disease

The prion protein can trigger the normal proteins in the brains to fold unusually. A prion disease affects both people and the animals and these prions are occasionally spread to people via the septic meat products. The most usual form of prion disease which affects individuals is the Creutzfeldt-Jakob disease (CJD) (Llewelyn et al., 418). The flawed proteins are transmitted by the contaminated and garnered human brain that produces electrode implants, dural grafts or the corneal grafts which may show up in the patient in the form of the sCJD sporadic variant. In this hereditary manifestation, a genetic transfiguration occurs on the PrP and PRNP gene variants. About fifteen percent of the CJD situations often get considered as emanating from ancestry.

The onset of Creutzfeldt-Jakob disease presumably occurs immediately after the consumption of the human growth hormones extracted from the pituitary glands of infected persons who had previously succumbed to the Creutzfeldt–Jacob illness (Llewelyn et al., 418). Since the documented occurrence of the disease in relation to the use of human growth hormones is relatively scanty and the data insignificant in light of modern scientific research, the probability of such an occurrence in it still remains high.

Imperatively, it remains scientifically and biologically plausible that humans can get the disease through the consumption of materials from the infected animals with some bovine forms of this disease. The suspected condition of the occurrence so far has been the vCJD with the case in Canada and the UK. However, there is fear that is based on the animal studies which show that consumption of beef or some beef products having prion elements may also lead to the development of the classic CJD. When the BSE materials infect humans, the subsequent disease can be called new variant CJD (nvCJD) (Llewelyn et al., 419).

Cannibalism has been associated to be a transmission device for the abnormal prions, which cause the disease called as kuru. The disease was once established primarily among some children and women belonging to a tribe found in Papua New Guinea (Will, 261). Though the men from this tribe ate a body of the dead and seldom got the infection, their women and the children that ate the fewer anticipated body portions, like the brains, were far more probable than the men to get the kuru from diseased tissues.

A report present by the Lancet medical paper indicated that the vCJD is likely to be transmitted through blood transfusion. This finding upset the healthcare administrators due to a larger widespread of this disease that may occur sooner. A blood examination for a vCJD infection can be probable but cannot be accessible for the selection blood donation. A significant limit exists to protect some blood supply. Many countries have shown up to the prevention of the blood donation from individuals that have the virus to limit the transmission of the disease in the world.

The risk of CJD at some point in the American history caused the FDA to indefinitely ban sperm donation because of fear of human transmission. It was evident that the transmission of the disease was probably through the transmission of sperms from an infected person to a healthy one. Although the research was clear concerning the transmission of the disease, it did not state if it could be transmitted by sexual contacts.

Relationship with Animal Prion Diseases

There exist similarities and difference between the CJD in humans and the other prion diseases among the animal. The similarities are based on the forms of transmission and the symptoms shown by the affected organisms. There is a strong evidence showing that the agent liable for the bovine spongiform encephalopathy (BSE) in some cows, frequently termed “mad cow disease,” is the same that is still responsible for the one type of CJD among the humans, which is known as “variant CJD.” BSE is shown to affected cows in the world, especially in the UK. The growth of the uncontrolled prion proteins that are misfolded protein is a common characteristic transmission of spongiform encephalopathies like scrapie found in sheep and the Creutzfeldt-Jakob disease (CJD).

The virus in both organisms is carried in the body of the dead organism and is transmitted to the healthy ones through the digestive system. The transmission process is similar in both the animals characterized by the same symptoms of the attack. However, in both cases the disease is harmful and communicable killing many organisms at a time, research has shown that many people and animals died in the UK between 19th and 20th centuries. It is vital to note that the disease can be transmitted from human beings to animals and from animals to the humans. The process equally involves the feeding on the dead matter of a deceased body. The control measures for both conditions are similar due to the similarities in the transmission processes.

Difficulties Encountered In Sterilizing Equipment Contaminated by (CJD)

Transmission of the prion diseases via the medical equipment as remained an ever-present risk in many test center and medical amenities in the world today. There have been many instances in which the sterilization process has caused transmission of the disease to the healthy and laboratory professionals involved in the sterilization process (Webb, Sidney & Arthur 85). Firstly, the amenities which lack decisive prion sterilization procedures for unprotected medical tools both jeopardize the lab personnel and endanger imminent patients who need to be treated using the equipment once it is processed.

The availability of improper machines to fully sterilize the contaminated equipment is a great challenge in the sterilization process. Some countries that lack the advanced technologies to fully sterilize the contaminated tools remain at risk of further transmissions. The machines often do not function well which results in harmful effects on the health of the health practitioners.

The disease is communicable and thus able to be transmitted from one individual to another, this characteristic creates fear in the sterilization process which may increase the probability of further transmission.

Conclusion

The emerging zoonotic illnesses cannot be assumed to be a simple one which consists the sociocultural concerns due to their nasty and fearful features. Similarly, BSE and vCJD are the distinctive emerging epidemics after AIDS. The causal agents, transmission processes and the forms of treatments required by the victims are still under study as shown from the recent researches. Conversely, some new facts on this pathogenesis of the diseases are found each year; and hoped, based on the experiences from the EU, that the vCJD and BSE will be controlled, while their occurrence is be lowered progressively. However, to reduce further risks from the transmission of the diseases, some stern cautionary laws have to be practiced because prevention is outlined as the most operational method of controlling these evolving diseases that remain unusual from the recent past.

Works Cited

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Gendoo, Deena. Bioinformatic Sequence and Structural Analysis for Amyloidogenicity in Prions and Other Proteins. 2012.

Llewelyn, C. A., et al. "Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion." The Lancet 363.9407 (2004): 417-421.

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